ID A0A434AVV5_9BACT Unreviewed; 462 AA.
AC A0A434AVV5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE RecName: Full=Aminopeptidase {ECO:0000256|PIRNR:PIRNR005700};
GN ORFNames=DLK05_07975 {ECO:0000313|EMBL:RUT78504.1};
OS Ancylomarina longa.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Marinifilaceae;
OC Ancylomarina.
OX NCBI_TaxID=2487017 {ECO:0000313|EMBL:RUT78504.1, ECO:0000313|Proteomes:UP000282985};
RN [1] {ECO:0000313|EMBL:RUT78504.1, ECO:0000313|Proteomes:UP000282985}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T3-2 S1-C {ECO:0000313|EMBL:RUT78504.1,
RC ECO:0000313|Proteomes:UP000282985};
RA Fu T.;
RT "Parancylomarina longa gen. nov., sp. nov., isolated from sediments of
RT southern Okinawa.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase C1 family.
CC {ECO:0000256|PIRNR:PIRNR005700}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RUT78504.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; RJJX01000008; RUT78504.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A434AVV5; -.
DR OrthoDB; 1111399at2; -.
DR Proteomes; UP000282985; Unassembled WGS sequence.
DR GO; GO:0070005; F:cysteine-type aminopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00585; Peptidase_C1B; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR025660; Pept_his_AS.
DR InterPro; IPR004134; Peptidase_C1B.
DR PANTHER; PTHR10363; BLEOMYCIN HYDROLASE; 1.
DR PANTHER; PTHR10363:SF2; BLEOMYCIN HYDROLASE; 1.
DR Pfam; PF03051; Peptidase_C1_2; 1.
DR PIRSF; PIRSF005700; PepC; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|PIRNR:PIRNR005700};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR005700};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PIRNR:PIRNR005700};
KW Reference proteome {ECO:0000313|Proteomes:UP000282985};
KW Signal {ECO:0000256|SAM:SignalP};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807,
KW ECO:0000256|PIRNR:PIRNR005700}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..462
FT /note="Aminopeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019126116"
FT ACT_SITE 92
FT /evidence="ECO:0000256|PIRSR:PIRSR005700-1"
FT ACT_SITE 385
FT /evidence="ECO:0000256|PIRSR:PIRSR005700-1"
FT ACT_SITE 407
FT /evidence="ECO:0000256|PIRSR:PIRSR005700-1"
SQ SEQUENCE 462 AA; 53114 MW; 623C665C3047299B CRC64;
MKKIVFFSVL VFAFCGITKA QNNGTIDAKM LNEIRSGFTL DASAKAAQNA ITNAESLRDL
SLNREKIGKI DHYFKYRVEV KGITDQKSSG RCWMFTSMNT IRPQAIKKFN LTSFDFSHNY
NYFWDLFEKS NLFLDNIIAT ADQDIQDREV VNYFKSPVDD GGVWNSFFNV AKKYGLVPAS
VMPETKMSNK TYELTRLINE KLRGEAYKIR MMIAAKDANK DIQQAKVNAL KSVYRMLALS
LGVPPTEFTW RYKDADGKIS ELKKYTPIEF LEVVAPDFAK TEQIMIMNDP TRAYYKVYEI
KNYRNVKEGI NWTYLNLPNK DIKSFALASI KNNEPMYASC DVGKQHNRKA GVMDVNTYDY
ASLFGVDFDM DKKARILTRQ SGSSHAMALI GVDVDENDVP VKWEFENSWG SSAGDKGYLT
FTDAWFNEYM FRIVINKKYL NEKAIKALQS KPILLPVWDY MF
//
